CNTN3_HUMAN
ID CNTN3_HUMAN Reviewed; 1028 AA.
AC Q9P232; B9EK50; Q9H039;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Contactin-3;
DE AltName: Full=Brain-derived immunoglobulin superfamily protein 1;
DE Short=BIG-1;
DE AltName: Full=Plasmacytoma-associated neuronal glycoprotein;
DE Flags: Precursor;
GN Name=CNTN3; Synonyms=KIAA1496, PANG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-708.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-1028.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 984-1028.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11013081; DOI=10.1006/geno.2000.6310;
RA Kamei Y., Takeda Y., Teramoto K., Tsutsumi O., Taketani Y., Watanabe K.;
RT "Human NB-2 of the contactin subgroup molecules: chromosomal localization
RT of the gene (CNTN5) and distinct expression pattern from other subgroup
RT members.";
RL Genomics 69:113-119(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489; ASN-860 AND ASN-931.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP INTERACTION WITH PTPRG.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
RN [8]
RP STRUCTURE BY NMR OF 893-996.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the fourth FN3 domain of KIAA1496 protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Has some neurite outgrowth-promoting activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In brain, it is expressed in frontal lobe,
CC occipital lobe, cerebellum and amygdala. {ECO:0000269|PubMed:11013081}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; AC016950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150608; AAI50609.1; -; mRNA.
DR EMBL; AB040929; BAA96020.1; -; mRNA.
DR EMBL; AL512746; CAC21671.1; -; mRNA.
DR CCDS; CCDS33790.1; -.
DR RefSeq; NP_065923.1; NM_020872.2.
DR RefSeq; XP_005264814.1; XM_005264757.3.
DR RefSeq; XP_016861996.1; XM_017006507.1.
DR PDB; 1WJ3; NMR; -; A=893-996.
DR PDBsum; 1WJ3; -.
DR AlphaFoldDB; Q9P232; -.
DR SMR; Q9P232; -.
DR IntAct; Q9P232; 4.
DR MINT; Q9P232; -.
DR STRING; 9606.ENSP00000263665; -.
DR GlyConnect; 1931; 10 N-Linked glycans (9 sites).
DR GlyGen; Q9P232; 13 sites, 10 N-linked glycans (9 sites).
DR iPTMnet; Q9P232; -.
DR PhosphoSitePlus; Q9P232; -.
DR BioMuta; CNTN3; -.
DR DMDM; 296439395; -.
DR MassIVE; Q9P232; -.
DR PaxDb; Q9P232; -.
DR PeptideAtlas; Q9P232; -.
DR PRIDE; Q9P232; -.
DR ProteomicsDB; 83720; -.
DR Antibodypedia; 1216; 165 antibodies from 24 providers.
DR DNASU; 5067; -.
DR Ensembl; ENST00000263665.7; ENSP00000263665.6; ENSG00000113805.9.
DR GeneID; 5067; -.
DR KEGG; hsa:5067; -.
DR MANE-Select; ENST00000263665.7; ENSP00000263665.6; NM_020872.3; NP_065923.1.
DR UCSC; uc003dpm.2; human.
DR CTD; 5067; -.
DR DisGeNET; 5067; -.
DR GeneCards; CNTN3; -.
DR HGNC; HGNC:2173; CNTN3.
DR HPA; ENSG00000113805; Tissue enhanced (brain).
DR MIM; 601325; gene.
DR neXtProt; NX_Q9P232; -.
DR OpenTargets; ENSG00000113805; -.
DR PharmGKB; PA26687; -.
DR VEuPathDB; HostDB:ENSG00000113805; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160282; -.
DR HOGENOM; CLU_005756_0_0_1; -.
DR InParanoid; Q9P232; -.
DR OMA; HKLMGAR; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q9P232; -.
DR TreeFam; TF351103; -.
DR PathwayCommons; Q9P232; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q9P232; -.
DR BioGRID-ORCS; 5067; 6 hits in 1065 CRISPR screens.
DR ChiTaRS; CNTN3; human.
DR EvolutionaryTrace; Q9P232; -.
DR GeneWiki; CNTN3; -.
DR GenomeRNAi; 5067; -.
DR Pharos; Q9P232; Tbio.
DR PRO; PR:Q9P232; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9P232; protein.
DR Bgee; ENSG00000113805; Expressed in Brodmann (1909) area 23 and 147 other tissues.
DR Genevisible; Q9P232; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1002
FT /note="Contactin-3"
FT /id="PRO_0000014705"
FT PROPEP 1003..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014706"
FT DOMAIN 26..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..313
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..497
FT /note="Ig-like C2-type 5"
FT DOMAIN 499..593
FT /note="Ig-like C2-type 6"
FT DOMAIN 600..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 703..800
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..901
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 902..998
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 684..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1002
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 913
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 521..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VARIANT 630
FT /note="S -> N (in dbSNP:rs626578)"
FT /id="VAR_019906"
FT VARIANT 708
FT /note="N -> S (in dbSNP:rs626578)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_056042"
FT STRAND 918..922
FT /evidence="ECO:0007829|PDB:1WJ3"
FT STRAND 930..932
FT /evidence="ECO:0007829|PDB:1WJ3"
FT STRAND 935..946
FT /evidence="ECO:0007829|PDB:1WJ3"
FT STRAND 951..963
FT /evidence="ECO:0007829|PDB:1WJ3"
FT STRAND 970..980
FT /evidence="ECO:0007829|PDB:1WJ3"
FT STRAND 989..991
FT /evidence="ECO:0007829|PDB:1WJ3"
SQ SEQUENCE 1028 AA; 112883 MW; 575945CD75D21844 CRC64;
MMFPWKQLIL LSFIGCLGGE LLLQGPVFIK EPSNSIFPVG SEDKKITLHC EARGNPSPHY
RWQLNGSDID MSMEHRYKLN GGNLVVINPN RNWDTGTYQC FATNSLGTIV SREAKLQFAY
LENFKTKMRS TVSVREGQGV VLLCGPPPHS GELSYAWIFN EYPSFVEEDS RRFVSQETGH
LYISKVEPSD VGNYTCVVTS MVTNARVLGS PTPLVLRSDG VMGEYEPKIE VQFPETLPAA
KGSTVKLECF ALGNPIPQIN WRRSDGLPFS SKIKLRKFSG VLEIPNFQQE DAGSYECIAE
NSRGKNVARG RLTYYAKPHW VQLIKDVEIA VEDSLYWECR ASGKPKPSYR WLKNGAALVL
EERTQIENGA LTISNLSVTD SGMFQCIAEN KHGLVYSSAE LKVVASAPDF SKNPMKKLVQ
VQVGSLVSLD CKPRASPRAL SSWKKGDVSV QEHERISLLN DGGLKIANVT KADAGTYTCM
AENQFGKANG TTHLVVTEPT RITLAPSNMD VSVGESVILP CQVQHDPLLD IIFTWYFNGA
LADFKKDGSH FEKVGGSSSG DLMIRNIQLK HSGKYVCMVQ TGVDSVSSAA DLIVRGSPGP
PENVKVDEIT DTTAQLSWKE GKDNHSPVIS YSIQARTPFS VGWQTVTTVP EVIDGKTHTA
TVVELNPWVE YEFRVVASNK IGGGEPSLPS EKVRTEEAVP EVPPSEVNGG GGSRSELVIT
WDPVPEELQN GEGFGYVVAF RPLGVTTWIQ TVVTSPDTPR YVFRNESIVP YSPYEVKVGV
YNNKGEGPFS PVTTVFSAEE EPTVAPSQVS ANSLSSSEIE VSWNTIPWKL SNGHLLGYEV
RYWNGGGKEE SSSKMKVAGN ETSARLRGLK SNLAYYTAVR AYNSAGAGPF SATVNVTTKK
TPPSQPPGNV VWNATDTKVL LNWEQVKAME NESEVTGYKV FYRTSSQNNV QVLNTNKTSA
ELVLPIKEDY IIEVKATTDG GDGTSSEQIR IPRITSMDAR GSTSAISNVH PMSSYMPIVL
FLIVYVLW
